FAEHP_METBF
ID FAEHP_METBF Reviewed; 392 AA.
AC Q46DY5;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Bifunctional enzyme Fae/Hps {ECO:0000255|HAMAP-Rule:MF_01268};
DE Includes:
DE RecName: Full=5,6,7,8-tetrahydromethanopterin hydro-lyase {ECO:0000255|HAMAP-Rule:MF_01268};
DE EC=4.2.1.147 {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000269|PubMed:16075199};
DE AltName: Full=Formaldehyde-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199};
DE Short=Fae {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199};
DE Includes:
DE RecName: Full=3-hexulose-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199};
DE Short=HPS {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199};
DE EC=4.1.2.43 {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000269|PubMed:16075199};
DE AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase {ECO:0000255|HAMAP-Rule:MF_01268};
GN Name=faeB-hpsB {ECO:0000303|PubMed:16075199}; OrderedLocusNames=Mbar_A0935;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16075199; DOI=10.1007/s00203-005-0008-1;
RA Goenrich M., Thauer R.K., Yurimoto H., Kato N.;
RT "Formaldehyde activating enzyme (Fae) and hexulose-6-phosphate synthase
RT (Hps) in Methanosarcina barkeri: a possible function in ribose-5-phosphate
RT biosynthesis.";
RL Arch. Microbiol. 184:41-48(2005).
CC -!- FUNCTION: Catalyzes the condensation of formaldehyde with
CC tetrahydromethanopterin (H(4)MPT) to 5,10-
CC methylenetetrahydromethanopterin. {ECO:0000255|HAMAP-Rule:MF_01268,
CC ECO:0000269|PubMed:16075199}.
CC -!- FUNCTION: Catalyzes the reversible formation of ribulose-5-phosphate
CC and formaldehyde from 3-hexulose-6-phosphate. {ECO:0000255|HAMAP-
CC Rule:MF_01268, ECO:0000269|PubMed:16075199}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6,7,8-tetrahydromethanopterin + formaldehyde = 5,10-
CC methylenetetrahydromethanopterin + H2O; Xref=Rhea:RHEA:24678,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16842, ChEBI:CHEBI:57818,
CC ChEBI:CHEBI:58103; EC=4.2.1.147; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01268, ECO:0000269|PubMed:16075199};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate + formaldehyde = D-arabino-hex-3-ulose
CC 6-phosphate; Xref=Rhea:RHEA:25201, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:58121, ChEBI:CHEBI:58542; EC=4.1.2.43;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01268,
CC ECO:0000269|PubMed:16075199};
CC -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16075199}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the formaldehyde-
CC activating enzyme family. {ECO:0000255|HAMAP-Rule:MF_01268}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the HPS/KGPDC family.
CC HPS subfamily. {ECO:0000255|HAMAP-Rule:MF_01268}.
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DR EMBL; CP000099; AAZ69907.1; -; Genomic_DNA.
DR RefSeq; WP_011305956.1; NC_007355.1.
DR AlphaFoldDB; Q46DY5; -.
DR SMR; Q46DY5; -.
DR STRING; 269797.Mbar_A0935; -.
DR EnsemblBacteria; AAZ69907; AAZ69907; Mbar_A0935.
DR GeneID; 3627315; -.
DR KEGG; mba:Mbar_A0935; -.
DR eggNOG; arCOG00103; Archaea.
DR HOGENOM; CLU_701335_0_0_2; -.
DR OMA; LWDPPYL; -.
DR OrthoDB; 24053at2157; -.
DR UniPathway; UPA00293; -.
DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:InterPro.
DR GO; GO:0043801; F:hexulose-6-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd04726; KGPDC_HPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.230.60; -; 1.
DR HAMAP; MF_01268; Fae_Hps; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR020868; Fae/Hps.
DR InterPro; IPR014826; HCHO-activating_enzyme.
DR InterPro; IPR037075; HCHO-activating_enzyme_sf.
DR InterPro; IPR041710; HPS/KGPDC.
DR InterPro; IPR001754; OMPdeCOase_dom.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR Pfam; PF08714; Fae; 1.
DR Pfam; PF00215; OMPdecase; 1.
DR SMART; SM00934; OMPdecase; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR03126; one_C_fae; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Lyase; Multifunctional enzyme.
FT CHAIN 1..392
FT /note="Bifunctional enzyme Fae/Hps"
FT /id="PRO_0000235168"
FT REGION 1..161
FT /note="Formaldehyde-activating enzyme"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT REGION 162..392
FT /note="3-hexulose-6-phosphate synthase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT ACT_SITE 17
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 48
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01268"
SQ SEQUENCE 392 AA; 42415 MW; AE132C4FBBAC00A1 CRC64;
MFQIGEALMG QGAELAHVDL MIGDKGGPVG QAFANGLTQL SVGHTPLLSV IRPNLPPKPS
TLIIPKVTVK NMEQAGKIFG PAQAAVAKAV ADSVEEGVIS KDQVEEIVIV ASVFIHPDAQ
DYNKIYRYNY GATKLAIKRA LGGFPDINTV LEESNKSTHA IMGFKVTRLW DPPYLQVAFD
NPDIEFVQSA ISQIPKSDHV IIEAGTPLIK RYGMDVISRI REVRPDAFIV ADLKTLDTGN
LEARMVADAA GDAIVVSALA PISTIDKLIE EAHKTGIYAV MDTLNQQDPI SVLKQLKVMP
DVIELHRGID IEATEHAWGN IAEIKKIAPK ILVAVAGGVR LDKVPVALGQ GADILVVGRA
ITNSKDVREV AEQFINSLNK PEIDQFRVMT DF
